NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|737222679|ref|WP_035207341|]
View 

CmpA/NrtA family ABC transporter substrate-binding protein [Agrobacterium pusense]

Protein Classification

CmpA/NrtA family ABC transporter substrate-binding protein( domain architecture ID 10596738)

CmpA/NrtA family ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one of a variety of substrates, such as CmpA protein that binds bicarbonate and is involved in the active transport of bicarbonate; belongs to the type 2 periplasmic binding protein (PBP2) superfamily

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
32-290 1.17e-81

NMT1-like family; This family is closely related to the pfam09084 family.


:

Pssm-ID: 463863  Cd Length: 254  Bit Score: 251.88  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679   32 LRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMLGLGSNPSPTITPFSL 111
Cdd:pfam13379   8 LKLGFIPLTDAAPLIVAAEKGFFAKYGLTVELSKQASWAETRDALVAGELDAAHVLTPMPYLITLGIGGAKVPMIVLASL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  112 GRGGNAITLSTRLFDRMKavtglsetagalENAEALKRVLDDMRARGePPPTLGMTYPFSSHNYEFRYWLAAGGIHPDND 191
Cdd:pfam13379  88 NLNGQAITLANKYADKGV------------RDAAALKDLVGAYKASG-KPFKFAVTFPGSTHDLWLRYWLAAGGLDPDAD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  192 VKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWAANQQEAVGRLLTALDA 271
Cdd:pfam13379 155 VKLVVVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVKALIE 234
                         250       260
                  ....*....|....*....|
gi 737222679  272 AARWCDL-AENHDELSRALA 290
Cdd:pfam13379 235 ATRWLDAkPENRREAAKLLA 254
 
Name Accession Description Interval E-value
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
32-290 1.17e-81

NMT1-like family; This family is closely related to the pfam09084 family.


Pssm-ID: 463863  Cd Length: 254  Bit Score: 251.88  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679   32 LRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMLGLGSNPSPTITPFSL 111
Cdd:pfam13379   8 LKLGFIPLTDAAPLIVAAEKGFFAKYGLTVELSKQASWAETRDALVAGELDAAHVLTPMPYLITLGIGGAKVPMIVLASL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  112 GRGGNAITLSTRLFDRMKavtglsetagalENAEALKRVLDDMRARGePPPTLGMTYPFSSHNYEFRYWLAAGGIHPDND 191
Cdd:pfam13379  88 NLNGQAITLANKYADKGV------------RDAAALKDLVGAYKASG-KPFKFAVTFPGSTHDLWLRYWLAAGGLDPDAD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  192 VKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWAANQQEAVGRLLTALDA 271
Cdd:pfam13379 155 VKLVVVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVKALIE 234
                         250       260
                  ....*....|....*....|
gi 737222679  272 AARWCDL-AENHDELSRALA 290
Cdd:pfam13379 235 ATRWLDAkPENRREAAKLLA 254
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
32-269 1.46e-69

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 218.99  E-value: 1.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  32 LRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMLGlgsNPSPTITPFSL 111
Cdd:cd13553    2 LRIGYLPITDHAPLLVAKEKGFFEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYG---KGAPIKVVAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 112 GRGGNAITLSTRLfdrmkavtglsetagALENAEALKrvlddmrargepPPTLGMTYPFSSHNYEFRYWLAAGGIHPDND 191
Cdd:cd13553   79 HRNGSAIVVSKDS---------------GIKSVADLK------------GKTIAVPFPGSTHDVLLRYWLAAAGLDPGKD 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737222679 192 VKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWAANQQEAVGRLLTAL 269
Cdd:cd13553  132 VEIVVLPPPDMVAALAAGQIDAYCVGEPWNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKAL 209
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
17-352 2.43e-43

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 153.62  E-value: 2.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  17 APGAPARVGSDRQKILRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMl 96
Cdd:COG0715    9 LAACSAAAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAAR- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  97 glgSNPSPTITPFSLG-RGGNAITLSTRlfdrmKAVTGLSETAGalenaealKRVlddmrargeppptlgMTYPFSSHNY 175
Cdd:COG0715   88 ---AKGAPVKAVAALSqSGGNALVVRKD-----SGIKSLADLKG--------KKV---------------AVPGGSTSHY 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 176 EFRYWLAAGGIHPDnDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWA 255
Cdd:COG0715  137 LLRALLAKAGLDPK-DVEIVNLPPPDAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVASEDFL 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 256 ANQQEAVGRLLTALDAAARWCDlaENHDELSRALAdpRYIGAPEAIIRRVLAGEFSIDSRgnrrvidkyftfhgghANYP 335
Cdd:COG0715  216 EENPEAVKAFLRALLKAWAWAA--ANPDEAAAILA--KATGLDPEVLAAALEGDLRLDPP----------------LGAP 275
                        330
                 ....*....|....*..
gi 737222679 336 RQSQALWIYSQMIRWGQ 352
Cdd:COG0715  276 DPARLQRVADFLVELGL 292
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
171-291 8.03e-07

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 50.44  E-value: 8.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  171 SSHNYEFRYWLAAGgiHPDNDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGM 250
Cdd:TIGR01728 111 SGHDLLLRALLKAG--LSGDDVTILYLGPSDARAAFAAGQVDAWAIWEPWGSALVEEGGARVLANGEGIGLPGQPGFLVV 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 737222679  251 RPEWAANQQEAVGRLLTALDAAARWCDlaENHDELSRALAD 291
Cdd:TIGR01728 189 RREFAEAHPEQVQRVLKVLVKARKWAE--ENPEESAKILAK 227
 
Name Accession Description Interval E-value
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
32-290 1.17e-81

NMT1-like family; This family is closely related to the pfam09084 family.


Pssm-ID: 463863  Cd Length: 254  Bit Score: 251.88  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679   32 LRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMLGLGSNPSPTITPFSL 111
Cdd:pfam13379   8 LKLGFIPLTDAAPLIVAAEKGFFAKYGLTVELSKQASWAETRDALVAGELDAAHVLTPMPYLITLGIGGAKVPMIVLASL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  112 GRGGNAITLSTRLFDRMKavtglsetagalENAEALKRVLDDMRARGePPPTLGMTYPFSSHNYEFRYWLAAGGIHPDND 191
Cdd:pfam13379  88 NLNGQAITLANKYADKGV------------RDAAALKDLVGAYKASG-KPFKFAVTFPGSTHDLWLRYWLAAGGLDPDAD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  192 VKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWAANQQEAVGRLLTALDA 271
Cdd:pfam13379 155 VKLVVVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVKALIE 234
                         250       260
                  ....*....|....*....|
gi 737222679  272 AARWCDL-AENHDELSRALA 290
Cdd:pfam13379 235 ATRWLDAkPENRREAAKLLA 254
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
32-269 1.46e-69

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 218.99  E-value: 1.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  32 LRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMLGlgsNPSPTITPFSL 111
Cdd:cd13553    2 LRIGYLPITDHAPLLVAKEKGFFEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYG---KGAPIKVVAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 112 GRGGNAITLSTRLfdrmkavtglsetagALENAEALKrvlddmrargepPPTLGMTYPFSSHNYEFRYWLAAGGIHPDND 191
Cdd:cd13553   79 HRNGSAIVVSKDS---------------GIKSVADLK------------GKTIAVPFPGSTHDVLLRYWLAAAGLDPGKD 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737222679 192 VKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWAANQQEAVGRLLTAL 269
Cdd:cd13553  132 VEIVVLPPPDMVAALAAGQIDAYCVGEPWNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKAL 209
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
17-352 2.43e-43

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 153.62  E-value: 2.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  17 APGAPARVGSDRQKILRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVASMl 96
Cdd:COG0715    9 LAACSAAAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAAR- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  97 glgSNPSPTITPFSLG-RGGNAITLSTRlfdrmKAVTGLSETAGalenaealKRVlddmrargeppptlgMTYPFSSHNY 175
Cdd:COG0715   88 ---AKGAPVKAVAALSqSGGNALVVRKD-----SGIKSLADLKG--------KKV---------------AVPGGSTSHY 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 176 EFRYWLAAGGIHPDnDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMRPEWA 255
Cdd:COG0715  137 LLRALLAKAGLDPK-DVEIVNLPPPDAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVASEDFL 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 256 ANQQEAVGRLLTALDAAARWCDlaENHDELSRALAdpRYIGAPEAIIRRVLAGEFSIDSRgnrrvidkyftfhgghANYP 335
Cdd:COG0715  216 EENPEAVKAFLRALLKAWAWAA--ANPDEAAAILA--KATGLDPEVLAAALEGDLRLDPP----------------LGAP 275
                        330
                 ....*....|....*..
gi 737222679 336 RQSQALWIYSQMIRWGQ 352
Cdd:COG0715  276 DPARLQRVADFLVELGL 292
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
32-272 6.13e-18

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 81.95  E-value: 6.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  32 LRAGFIPLVDASVLIAAAEFGFAERE--GITLDLVKDVSWANARDRLAFRQFDIAHMLSPMPVasmLGLGSNPSP-TITP 108
Cdd:cd01008    2 VRIGYQAGPLAGPLIVAKEKGLFEKEkeGIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPAL---LAAAGGVPVvLIAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 109 FSLGRGGNAITLStrlfdRMKAVTGLSETAGalenaealKRVlddmrargeppptlGMTYPFSSHNYeFRYWLAAGGIhP 188
Cdd:cd01008   79 LSRSPNGNGIVVR-----KDSGITSLADLKG--------KKI--------------AVTKGTTGHFL-LLKALAKAGL-S 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 189 DNDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWpSAPEKVVGMRPEWAANQQEAVGRLLTA 268
Cdd:cd01008  130 VDDVELVNLGPADAAAALASGDVDAWVTWEPFLSLAEKGGDARIIVDGGGLP-YTDPSVLVARRDFVEENPEAVKALLKA 208

                 ....
gi 737222679 269 LDAA 272
Cdd:cd01008  209 LVEA 212
PBP2_sulfate_ester_like cd13555
Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This ...
181-304 1.50e-07

Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270273  Cd Length: 268  Bit Score: 52.34  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 181 LAAGGIHpDNDVKLVVVPPPLTSDALAAGAIDGFCVGAPWnIVAAERGVGRIVAAKQDLWPS-APEKVVGMRPEWAANQQ 259
Cdd:cd13555  131 LAKNGLS-EKDFKIVNLDAQDAQAALASGDVDAAFTGYEA-LKLEDQGAGKIIWSTKDKPEDwTTQSGVWARTDFIKENP 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 737222679 260 EAVGRLLTALDAAARWCDLAENHDEL----SRAladpryiGAPEAIIRR 304
Cdd:cd13555  209 DVVQRIVTALVKAARWVSQEENRDEYiqlwSRS-------GTPEELIKE 250
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
171-291 8.03e-07

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 50.44  E-value: 8.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  171 SSHNYEFRYWLAAGgiHPDNDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGM 250
Cdd:TIGR01728 111 SGHDLLLRALLKAG--LSGDDVTILYLGPSDARAAFAAGQVDAWAIWEPWGSALVEEGGARVLANGEGIGLPGQPGFLVV 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 737222679  251 RPEWAANQQEAVGRLLTALDAAARWCDlaENHDELSRALAD 291
Cdd:TIGR01728 189 RREFAEAHPEQVQRVLKVLVKARKWAE--ENPEESAKILAK 227
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
32-272 1.78e-06

Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 periplasmic binding protein fold; This subfamily is phylogenetically similar to ThiY, which is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270370 [Multi-domain]  Cd Length: 217  Bit Score: 48.54  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679  32 LRAGFIPLVDASVLIAAAEFGFAEREGITLDLVKDVSWANARDRLAFRQFDIAHMlspMPVASMLG------------LG 99
Cdd:cd13652    4 VKFGQIPISDFAPVYIAAEKGYFKEEGLDVEITRFASGAEILAALASGQVDVAGS---SPGASLLGalargadlkivaEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 100 SNPSPTITPFSL-GRGGNAITLSTRLFDRMKAVTGLSETAgalenaealkrvlddmrargeppptlgmtypfsshNYEFR 178
Cdd:cd13652   81 LGTTPGYGPFAIvVRADSGITSPADLVGKKIAVSTLTNIL-----------------------------------EYTTN 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 179 YWLAAGGIHPDnDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGvGRIVAAKQDLWPSAPEKVVGMRPEWAANQ 258
Cdd:cd13652  126 AYLKKNGLDPD-KVEFVEVAFPQMVPALENGNVDAAVLAEPFLSRARSSG-AKVVASDYADPDPHSQATMVFSADFAREN 203
                        250
                 ....*....|....
gi 737222679 259 QEAVGRLLTALDAA 272
Cdd:cd13652  204 PEVVKKFLRAYLEA 217
PBP2_DszB cd13554
Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 ...
178-303 2.34e-06

Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes DszB, which converts 2'-hydroxybiphenyl-2-sulfinate to 2-hydroxybiphenyl and sulfinate at the rate-limiting step of the microbial dibenzothiophene desulfurization pathway. The overall fold of DszB is highly similar to those of periplasmic substrate-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The DszB protein belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270272 [Multi-domain]  Cd Length: 246  Bit Score: 48.66  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 178 RYWLAAGGIHPDND--VKLVVVPP----PLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVGMR 251
Cdd:cd13554  116 GSWLARALLHNLEIggLDVEIVPIdspgRGQAAALDSGDIDALASWLPWATTLQATGGARPLVDLGLVEGNSYYSTWTVR 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 737222679 252 PEWAANQQEAVGRLLTALDAAARWcdlAENHDELSRALADPRYIGAPEAIIR 303
Cdd:cd13554  196 SDFIEQNPEAVKALVEALVRAGDW---IQAHPEAVVIIHAAEIGVSPGAVGR 244
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
190-307 1.17e-05

Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the sulfonate binding domains SsuA found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270275  Cd Length: 275  Bit Score: 46.90  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 190 NDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLWPSAPEKVVgmRPEWAANQQEAVGRLLTAL 269
Cdd:cd13557  130 DDIEPVYLSPADARAAFEQGQVDAWAIWDPYLAAAELTGGARVLADGEGLVNNRSFYLA--ARDFAKDNPEAIQIVLEEL 207
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 737222679 270 DAAARWcdLAENHDELSRALADprYIGAPEAIIRRVLA 307
Cdd:cd13557  208 NKAGEW--ANTNRDEAAKLLAE--SLGIDAVVLELAVA 241
PBP2_SsuA_like_4 cd13561
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
135-272 5.94e-05

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270279 [Multi-domain]  Cd Length: 212  Bit Score: 43.90  E-value: 5.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 135 SETAGALENAEALKRVLDDMRARgepppTLGMTYPFSSHNYEFRYWLAAGgIHPDnDVKLVVVPPPLTSDALAAGAIDGF 214
Cdd:cd13561   80 NATASLIVRADSGIASIADLKGK-----KIGTPSGTTADVALDLALRKAG-LSEK-DVQIVNMDPAEIVTAFTSGSVDAA 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737222679 215 CVGAPWNIVAAERGVG-RIVAAKQDLWPSAPekVVGM---RPEWAANQQEAVGRLLTALDAA 272
Cdd:cd13561  153 ALWAPNTATIKEKVPGaVELADNSDFGPDAA--VPGAwvaRNKYAEENPEELKKFLAALAEA 212
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
163-272 8.86e-05

Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270281 [Multi-domain]  Cd Length: 208  Bit Score: 43.38  E-value: 8.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 163 TLGMTYPFSSHnYEFRYWLAAGGIHpDNDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVGRIVAAKQDLwPS 242
Cdd:cd13563  102 TVAVEEGSVSH-FLLLNALEKAGLT-EKDVKIVNMTAGDAGAAFIAGQVDAAVTWEPWLSNALKRGKGKVLVSSADT-PG 178
                         90       100       110
                 ....*....|....*....|....*....|
gi 737222679 243 APEKVVGMRPEWAANQQEAVGRLLTALDAA 272
Cdd:cd13563  179 LIPDVLVVREDFIKKNPEAVKAVVKAWFDA 208
PBP2_SsuA_like_3 cd13559
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
151-286 3.33e-04

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270277  Cd Length: 258  Bit Score: 42.02  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737222679 151 LDDMRARgepppTLGMTYPFSSHNYEFRYwLAAGGIHPDNDVKLVVVPPPLTSDALAAGAIDGFCVGAPWNIVAAERGVG 230
Cdd:cd13559  116 LDDLKGK-----TVSVPFGSSAHGMLLRA-LDRAGLNPDTDVTIINQAPEVGGSALQANKIDAHADFVPFPELFPHRGIA 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 737222679 231 R-IVAAKQDLWPSAPEKVVgmRPEWAANQQEAVGRLLTALDAAARWcdLAENHDELS 286
Cdd:cd13559  190 RkLYDGSQTKVPTFHGIVV--DRDFAEKHPEVVVAYLRALIEAHRL--IREEPEAYS 242
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH